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Caveolin-1 interacts with the Gag precursor of murine leukaemia virus and modulates virus production

BACKGROUND: Retroviral Gag determines virus assembly at the plasma membrane and the formation of virus-like particles in intracellular multivesicular bodies. Thereby, retroviruses exploit by interaction with cellular partners the cellular machineries for vesicular transport in various ways. RESULTS:...

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Autores principales: Yu, Zheng, Beer, Christiane, Koester, Mario, Wirth, Manfred
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1570462/
https://www.ncbi.nlm.nih.gov/pubmed/16956408
http://dx.doi.org/10.1186/1743-422X-3-73
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author Yu, Zheng
Beer, Christiane
Koester, Mario
Wirth, Manfred
author_facet Yu, Zheng
Beer, Christiane
Koester, Mario
Wirth, Manfred
author_sort Yu, Zheng
collection PubMed
description BACKGROUND: Retroviral Gag determines virus assembly at the plasma membrane and the formation of virus-like particles in intracellular multivesicular bodies. Thereby, retroviruses exploit by interaction with cellular partners the cellular machineries for vesicular transport in various ways. RESULTS: The retroviral Gag precursor protein drives assembly of murine leukaemia viruses (MLV) at the plasma membrane (PM) and the formation of virus like particles in multivesicular bodies (MVBs). In our study we show that caveolin-1 (Cav-1), a multifunctional membrane-associated protein, co-localizes with Gag in a punctate pattern at the PM of infected NIH 3T3 cells. We provide evidence that Cav-1 interacts with the matrix protein (MA) of the Gag precursor. This interaction is mediated by a Cav-1 binding domain (CBD) within the N-terminus of MA. Interestingly, the CBD motif identified within MA is highly conserved among most other γ-retroviruses. Furthermore, Cav-1 is incorporated into MLV released from NIH 3T3 cells. Overexpression of a GFP fusion protein containing the putative CBD of the retroviral MA resulted in a considerable decrease in production of infectious retrovirus. Moreover, expression of a dominant-negative Cav-1 mutant affected retroviral titres significantly. CONCLUSION: This study demonstrates that Cav-1 interacts with MLV Gag, co-localizes with Gag at the PM and affects the production of infectious virus. The results strongly suggest a role for Cav-1 in the process of virus assembly.
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spelling pubmed-15704622006-09-21 Caveolin-1 interacts with the Gag precursor of murine leukaemia virus and modulates virus production Yu, Zheng Beer, Christiane Koester, Mario Wirth, Manfred Virol J Research BACKGROUND: Retroviral Gag determines virus assembly at the plasma membrane and the formation of virus-like particles in intracellular multivesicular bodies. Thereby, retroviruses exploit by interaction with cellular partners the cellular machineries for vesicular transport in various ways. RESULTS: The retroviral Gag precursor protein drives assembly of murine leukaemia viruses (MLV) at the plasma membrane (PM) and the formation of virus like particles in multivesicular bodies (MVBs). In our study we show that caveolin-1 (Cav-1), a multifunctional membrane-associated protein, co-localizes with Gag in a punctate pattern at the PM of infected NIH 3T3 cells. We provide evidence that Cav-1 interacts with the matrix protein (MA) of the Gag precursor. This interaction is mediated by a Cav-1 binding domain (CBD) within the N-terminus of MA. Interestingly, the CBD motif identified within MA is highly conserved among most other γ-retroviruses. Furthermore, Cav-1 is incorporated into MLV released from NIH 3T3 cells. Overexpression of a GFP fusion protein containing the putative CBD of the retroviral MA resulted in a considerable decrease in production of infectious retrovirus. Moreover, expression of a dominant-negative Cav-1 mutant affected retroviral titres significantly. CONCLUSION: This study demonstrates that Cav-1 interacts with MLV Gag, co-localizes with Gag at the PM and affects the production of infectious virus. The results strongly suggest a role for Cav-1 in the process of virus assembly. BioMed Central 2006-09-06 /pmc/articles/PMC1570462/ /pubmed/16956408 http://dx.doi.org/10.1186/1743-422X-3-73 Text en Copyright © 2006 Yu et al; licensee BioMed Central Ltd. https://creativecommons.org/licenses/by/2.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0 (https://creativecommons.org/licenses/by/2.0/) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
Yu, Zheng
Beer, Christiane
Koester, Mario
Wirth, Manfred
Caveolin-1 interacts with the Gag precursor of murine leukaemia virus and modulates virus production
title Caveolin-1 interacts with the Gag precursor of murine leukaemia virus and modulates virus production
title_full Caveolin-1 interacts with the Gag precursor of murine leukaemia virus and modulates virus production
title_fullStr Caveolin-1 interacts with the Gag precursor of murine leukaemia virus and modulates virus production
title_full_unstemmed Caveolin-1 interacts with the Gag precursor of murine leukaemia virus and modulates virus production
title_short Caveolin-1 interacts with the Gag precursor of murine leukaemia virus and modulates virus production
title_sort caveolin-1 interacts with the gag precursor of murine leukaemia virus and modulates virus production
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1570462/
https://www.ncbi.nlm.nih.gov/pubmed/16956408
http://dx.doi.org/10.1186/1743-422X-3-73
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